BMRB Entry 15259

Name: LactococcinGa in DPC and TFE
Published: 2008-02-21

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PDB ID: 2jpj
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15259
MolProbity Validation Chart

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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

LactococcinGa in DPC and TFE

Deposition date:

2007-05-22

Original release date:

2008-02-21

Authors:

Rogne, Per; Fimland, Gunnar; Nissen-Meyer, Jon; Kristiansen, Per

Citation:

Citation: Rogne, Per; Fimland, Gunnar; Nissen-Meyer, Jon; Kristiansen, Per. "Three-dimensional structure of the two peptides that constitutes the two-peptide bacteriocin Lactococcin G" Biochim. Biophys. Acta. 1784, 543-554 (2008).
PubMed: 18187052

Assembly members:

Assembly members:
lcnGa, polymer, 39 residues, 4317.912 Da.

Natural source:

Natural source: Common Name: Lactococcus lactis Taxonomy ID: 1358 Superkingdom: Bacteria Kingdom: not available Genus/species: Lactococcus lactis

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pGEV2

Entity Sequences (FASTA):

Entity Sequences (FASTA):
lcnGa: GTWDDIGQGIGRVAYWVGKA LGNLSDVNQASRINRKKKH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
- assigned_chem_shift_list_2

Data type	Count
15N chemical shifts	91
1H chemical shifts	506

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	lcnGa	1

Entities:

Entity 1, lcnGa 39 residues - 4317.912 Da.

1

GLY

THR

TRP

ASP

ILE

GLY

GLN

GLY

ILE

2

GLY

ARG

VAL

ALA

TYR

TRP

VAL

GLY

LYS

ALA

3

LEU

GLY

ASN

LEU

SER

ASP

VAL

ASN

GLN

ALA

4

SER

ARG

ILE

ASN

ARG

LYS

HIS

Samples:

lcnGa_DPC: lcnGa, [U-15N], 1 mM; DPC, [U-2H], 200 mM; TFA 0.1%; D2O 10%; DSS 0.2 mM

lcnGaTFE: lcnG a TFE, [U-15N], 1 mM; TFE, [U-2H], 90%; TFA 0.1%; DSS 0.2 mM

25C: pH: 2.8; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	lcnGa_DPC	isotropic	25C
2D 1H-1H NOESY	lcnGa_DPC	isotropic	25C
2D 1H-1H TOCSY	lcnGa_DPC	isotropic	25C
3D 1H-15N NOESY	lcnGa_DPC	isotropic	25C
3D 1H-15N TOCSY	lcnGa_DPC	isotropic	25C
2D 1H-15N HSQC	lcnGaTFE	isotropic	25C
2D 1H-1H TOCSY	lcnGaTFE	isotropic	25C
2D 1H-1H NOESY	lcnGaTFE	isotropic	25C
3D 1H-15N TOCSY	lcnGaTFE	isotropic	25C
3D 1H-15N NOESY	lcnGaTFE	isotropic	25C

Software:

VNMR, Varian - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

CARA v1.4.1, Keller and Wuthrich - chemical shift assignment, data analysis

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

TALOS, Cornilescu, Delaglio and Bax - torsion angle prediction

Molmol v2k.2, Koradi, Billeter and Wuthrich - RMSD value calculation, Structure visualization

TOPSPIN v1.3, Bruker Biospin - collection, processing

NMR spectrometers:

Varian INOVA 600 MHz
Bruker Avance 600 MHz